Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8335211 | International Journal of Biological Macromolecules | 2011 | 6 Pages |
Abstract
Endo-1,3(4)-β-glucanase (EC 3.2.1.6) from Vigna aconitifolia sprouts was purified to 14.5 fold by gel filtration and ion-exchange chromatography. The enzyme was found to be a glycoprotein, its activity was Ca2+ dependent and specific for β-1,3 linkages in different polysaccharides. The Km value of the enzyme was estimated to be 3.0 mg mlâ1 for β-d-glucan as substrate. Circular dichroism studies revealed 8% α-helix, 48% β-pleated and 44% random coil in its secondary structure. Purified β-glucanase was then successfully co-immobilized with glucose oxidase in agarose-chitosan beads, showing better immobilization yield, operational range and stability as compared with the crude β-glucanase beads. The immobilized β-glucanase was successfully used for mini-bioreactor fabrication.
Keywords
PBSInternational Union of Biochemistry and Molecular BiologyIUBMBDNSAFIAVigna aconitifoliaADTDEAEBSAβ-Glucanasebovine serum albuminGlucose oxidasediethyl amino ethylEDTAEthylene diamine tetra acetic acidSDS-PAGESodium dodecyl sulfate polyacrylamide gel electrophoresisImmobilizationFlow injection analysisCharacterizationGODDinitrosalicylic ACIDcircular dichroismPhosphate buffered salinePurification
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Authors
Rakesh Mohan Kestwal, Dipali Bagal-Kestwal, Been Huang Chiang,